analysis of crystal structure of the globular C-terminal domain of human CblD, which is sufficient for its interaction with MMADHC or CblC (zeige CBLC Proteine), and for supporting the cytoplasmic cobalamin trafficking pathway

specific regions of MMADHC are involved in differential regulation of adenosylcobalamin and methylcobalamin synthesis

The function of MMADHC is exerted through its structured C-terminal domain via interactions with MMACHC (zeige MMACHC Proteine).

MMADHC mutations are associated with methylmalonic aciduria and homocystinuria.

MMADHC was confirmed as a binding partner for MMACHC (zeige MMACHC Proteine) both in vitro (SPR (zeige SPR Proteine)) and in vivo (bacterial two-hybrid system).

mutations in a gene designated MMADHC (currently named C2orf25) are responsible for the cblD defect in vitamin B12 (zeige NDUFB3 Proteine) metabolism; various mutations are associated with each of the three biochemical phenotypes of the disorder

Protein Überblick

This gene encodes a mitochondrial protein that is involved in an early step of vitamin B12 metabolism. Vitamin B12 (cobalamin) is essential for normal development and survival in humans. Mutations in this gene cause methylmalonic aciduria and homocystinuria type cblD (MMADHC), a disorder of cobalamin metabolism that is characterized by decreased levels of the coenzymes adenosylcobalamin and methylcobalamin. Pseudogenes have been identified on chromosomes 11 and X.